Search results for "PHOSPHATE"

showing 10 items of 1874 documents

Functional cysteine-less subunits of the transporter associated with antigen processing (TAP1 and TAP2) by de novo gene assembly

2002

AbstractWithin the adaptive immune system the transporter associated with antigen processing (TAP) plays a pivotal role in loading of peptides onto major histocompatibility (MHC) class I molecules. As a central tool to investigate the structure and function of the TAP complex, we created cysteine-less human TAP subunits by de novo gene synthesis, replacing all 19 cysteines in TAP1 and TAP2. After expression in TAP-deficient human fibroblasts, cysteine-less TAP1 and TAP2 are functional with respect to adenosine triphosphate (ATP)-dependent peptide transport and inhibition by ICP47 from herpes simplex virus. Cysteine-less TAP1 and TAP2 restore maturation and intracellular trafficking of MHC c…

Models MolecularBiophysicsBiological Transport ActiveBiologyMajor histocompatibility complexTransfectionBiochemistryCell Linechemistry.chemical_compoundAdenosine TriphosphateStructural BiologyATP Binding Cassette Transporter Subfamily B Member 3Cysteine-scanning mutagenesisMHC class IGeneticsHumansCysteineATP Binding Cassette Transporter Subfamily B Member 2Molecular BiologyAntigen PresentationAntigen processingHistocompatibility Antigens Class ICell BiologyTransporter associated with antigen processingMolecular biologyRecombinant ProteinsCell biologyProtein SubunitschemistryAmino Acid SubstitutionAntigen processingPeptide transportMembrane proteinbiology.proteinAdenosine triphosphate-binding cassette transporterTAP2ATP-Binding Cassette TransportersTAP1Adenosine triphosphateFEBS Letters
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Mechanistic insights into the phosphoryl transfer reaction in cyclin-dependent kinase 2: a QM/MM study

2019

AbstractCyclin-dependent kinase 2 (CDK2) is an important member of the CDK family exerting its most important function in the regulation of the cell cycle. It catalyzes the transfer of the gamma phosphate group from an ATP (adenosine triphosphate) molecule to a Serine/Threonine residue of a peptide substrate. Due to the importance of this enzyme, and protein kinases in general, a detailed understanding of the reaction mechanism is desired. Thus, in this work the phosphoryl transfer reaction catalyzed by CDK2 was revisited and studied by means of hybrid quantum mechanics/molecular mechanics (QM/MM) calculations. Our results show that the base-assisted mechanism is preferred over the substrat…

Models MolecularComposite ParticlesProtein ConformationPhysical ChemistryBiochemistry01 natural sciencesSubstrate Specificitychemistry.chemical_compoundPhosphorylationPost-Translational ModificationFree Energy0303 health sciencesMultidisciplinarybiologyKinasePhysicsQChemical ReactionsRChemistryReaction DynamicsPhysical SciencesThermodynamicsMedicineProtonsResearch ArticleChemical ElementsAtomsStereochemistryScienceMolecular Dynamics Simulation010402 general chemistryMolecular mechanicsReactantsQM/MMStructure-Activity Relationship03 medical and health sciencesCyclin-dependent kinaseParticle PhysicsNuclear PhysicsNucleons030304 developmental biologyChemical BondingCyclin-Dependent Kinase 2Cyclin-dependent kinase 2Biology and Life SciencesProteinsActive siteHydrogen BondingTransition StateBond order0104 chemical sciencesOxygenModels Chemicalchemistrybiology.proteinQuantum TheoryAdenosine triphosphate
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Insights into the catalytic mechanism of human sEH phosphatase by site-directed mutagenesis and LC-MS/MS analysis

2008

We have recently reported that human soluble epoxide hydrolase (sEH) is a bifunctional enzyme with a novel phosphatase enzymatic activity. Based on a structural relationship with other members of the haloacid dehalogenase superfamily, the sEH N-terminal phosphatase domain revealed four conserved sequence motifs, including the proposed catalytic nucleophile D9, and several other residues potentially implicated in substrate turnover and/or Mg(2+) binding. To enlighten the catalytic mechanism of dephosphorylation, we constructed sEH phosphatase active-site mutants by site-directed mutagenesis. A total of 18 mutants were constructed and recombinantly expressed in Escherichia coli as soluble pro…

Models MolecularEpoxide hydrolase 2Molecular Sequence DataPhosphatase10050 Institute of Pharmacology and Toxicology610 Medicine & healthMass SpectrometryPhosphatesDephosphorylation1315 Structural BiologyProtein structureStructural Biology1312 Molecular BiologyHumansPhosphofructokinase 2Amino Acid SequenceBinding siteProtein Structure QuaternarySite-directed mutagenesisMolecular BiologyEpoxide HydrolasesBinding SitesChemistrySubstrate (chemistry)Phosphoric Monoester HydrolasesRecombinant ProteinsProtein Structure TertiaryProtein SubunitsBiochemistryMutagenesis Site-Directed570 Life sciences; biologyDimerizationSequence AlignmentChromatography Liquid
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Design, Synthesis, and Biological Evaluation of 3,4-Diarylmaleimides as Angiogenesis Inhibitors

2006

The new analogue 2 of combretastatin A-4 was discovered to be an inhibitor of tubulin polymerization with an IC50 of 7.6 microM and reduced angiogenesis in the in vivo chick embryo model. Interestingly, in a series of 2,3-diarylmaleimides closely related to this lead, no other compound was found to be active in the tubulin polymerization assay. However, by screening in the in vivo chick embryo assay 10 was identified as a potent angiogenesis inhibitor indicating an alternative target. Indeed, molecular modeling studies suggest a reasonable binding mode of 10 at the ATP-binding site of the model kinase CDK2. Motivated by these results, analogues of 10 were screened for inhibitory activity in…

Models MolecularIndolesanimal structuresAngiogenesisAngiogenesis InhibitorsChick EmbryoIn Vitro TechniquesMaleimidesStructure-Activity Relationshipchemistry.chemical_compoundAdenosine TriphosphateIn vivoDrug DiscoveryAnimalsStructure–activity relationshipPyrrolesBinding siteCombretastatinBinding SitesbiologyChemistryKinaseCyclin-dependent kinase 2Vascular Endothelial Growth Factor Receptor-2Angiogenesis inhibitorBiochemistryDrug Designbiology.proteinMolecular MedicineJournal of Medicinal Chemistry
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Aryl-bis-(scorpiand)-aza receptors differentiate between nucleotide monophosphates by a combination of aromatic, hydrogen bond and electrostatic inte…

2014

Bis-polyaza pyridinophane scorpiands bind nucleotides in aqueous medium with 10–100 micromolar affinity, predominantly by electrostatic interactions between nucleotide phosphates and protonated aliphatic amines and assisted by aromatic stacking interactions. The pyridine-scorpiand receptor showed rare selectivity toward CMP with respect to other nucleotides, whereby two orders of magnitude affinity difference between CMP and UMP was the most appealing. The phenanthroline-scorpiand receptor revealed at pH 5 strong selectivity toward AMP with respect to other NMPs, based on the protonation of adenine heterocyclic N1. The results stress that the efficient recognition of small biomolecules with…

Models MolecularMacrocyclic CompoundsMagnetic Resonance Spectroscopyscorpiand receptor; nucleotide recognition; NMR; fluorescenceStereochemistryStatic ElectricityStackingProtonation010402 general chemistry01 natural sciencesBiochemistryPhosphateschemistry.chemical_compoundMoietyNucleotidePhysical and Theoretical Chemistrychemistry.chemical_classificationAza CompoundsMolecular Structure010405 organic chemistryHydrogen bondChemistryNucleotidesPhysicsArylBiomoleculeOrganic ChemistryHydrogen BondingHydrogen-Ion Concentration0104 chemical sciencesChemistrySelectivityOrganicbiomolecular chemistry
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Conformational response to ligand binding in phosphomannomutase2: insights into inborn glycosylation disorder.

2014

Background: Mutations in phosphomannomutase2 cause glycosylation disorder, a disease without a cure that will largely benefit from accurate ligand-bound models. Results: We obtained two models of phospomannomutase2 bound to glucose 1,6-bisphosphate and validated them with limited proteolysis. Conclusion: Ligand binding induces a large conformational transition in PMM2. Significance: We produce and validate closed-form models of PMM2 that represent a starting point for rational drug discovery.

Models MolecularPELEGlycosylationProtein Conformation1Molecular Sequence DataGlucose-6-PhosphateGlycosylation Inhibitor6-bisphosphate; PELE; computer modeling; drug discovery; glycosylation; glycosylation inhibitor; ligand-binding protein; phosphomannomutaseLigandsDrug DiscoveryAnimalsHumansAmino Acid Sequence16-BisphosphateProtein UnfoldingTemperatureLigand-binding Proteinphosphomannomutase 2 and mass spectrometryPhosphotransferases (Phosphomutases)PhosphomannomutaseMutationProteolysisMetabolism Inborn ErrorsMolecular BiophysicsPeptide HydrolasesProtein BindingComputer ModelingThe Journal of biological chemistry
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Effect of ATP Binding and Hydrolysis on Dynamics of Canine Parvovirus NS1▿ †

2010

ABSTRACT The replication protein NS1 is essential for genome replication and protein production in parvoviral infection. Many of its functions, including recognition and site-specific nicking of the viral genome, helicase activity, and transactivation of the viral capsid promoter, are dependent on ATP. An ATP-binding pocket resides in the middle of the modular NS1 protein in a superfamily 3 helicase domain. Here we have identified key ATP-binding amino acid residues in canine parvovirus (CPV) NS1 protein and mutated amino acids from the conserved A motif (K406), B motif (E444 and E445), and positively charged region (R508 and R510). All mutations prevented the formation of infectious viruse…

Models MolecularParvovirus CaninevirusesImmunologyMolecular Sequence DataPlasma protein bindingViral Nonstructural ProteinsMicrobiologyCell Linechemistry.chemical_compoundAdenosine TriphosphateDogsVirologyAnimalsAmino Acid SequenceBinding siteBinding SitesbiologyHydrolysisDNA replicationHelicaseFluorescence recovery after photobleachingFusion proteinMolecular biologyGenome Replication and Regulation of Viral Gene ExpressionProtein Structure TertiaryViral replicationchemistryBiochemistryAmino Acid SubstitutionInsect Sciencebiology.proteinCatsMutagenesis Site-DirectedSequence AlignmentDNAProtein Binding
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A phenoxo-bridged dicopper(ii) complex as a model for phosphatase activity: mechanistic insights from a combined experimental and computational study

2017

A μ-phenoxo-bis(μ2-1,3-acetato)-bridged dicopper(II) complex [CuII2(L1)(μ-O2CMe)2][NO3] (1) has been synthesized from the perspective of modeling phosphodiesterase activity. Structural characterization was done initially with 1·3Et2O (vapour diffusion of Et2O into MeOH solution of 1; poor crystal quality) and finally with its perchlorate salt [CuII2(L1)(μ-O2CMe)2][ClO4]·1.375MeCN·0.25H2O, crystallized from vapour diffusion of n-pentane into a MeCN–MeOH mixture (comparatively better crystal quality). An asymmetric unit of such a crystal contains two independent molecules of compositions [CuII2(L1)(μ-O2CMe)2][ClO4] and [CuII2(L1)(μ-O2CMe)2(MeCN)][ClO4] (coordinated MeCN with 0.75 occupancy), …

Models MolecularReaction mechanismStereochemistryMolecular ConformationLigands010402 general chemistry01 natural sciencesPhosphateslaw.inventionCatalysisInorganic ChemistryCrystalMetalchemistry.chemical_compoundBiomimetic MaterialsCoordination ComplexeslawMoleculeCrystallizationAcetonitrile010405 organic chemistryHydrolysisMagnetic PhenomenaTemperaturePhosphoric Monoester Hydrolases0104 chemical sciencesSolventKineticsCrystallographychemistryvisual_artvisual_art.visual_art_mediumCopperDalton Transactions
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Reversed Enantioselectivity of Diisopropyl Fluorophosphatase against Organophosphorus Nerve Agents by Rational Design

2009

Diisopropyl fluorophosphatase (DFPase) from Loligo vulgaris is an efficient and robust biocatalyst for the hydrolysis of a range of highly toxic organophosphorus compounds including the nerve agents sarin, soman, and cyclosarin. In contrast to the substrate diisopropyl fluorophosphate (DFP) the nerve agents possess an asymmetric phosphorus atom, which leads to pairs of enantiomers that display markedly different toxicities. Wild-type DFPase prefers the less toxic stereoisomers of the substrates which leads to slower detoxification despite rapid hydrolysis. Enzyme engineering efforts based on rational design yielded two quadruple enzyme mutants with reversed enantioselectivity and overall en…

Models MolecularSarinStereochemistryRational designCyclosarinStereoisomerismGeneral ChemistryNervous SystemBiochemistryCatalysisKineticschemistry.chemical_compoundOrganophosphorus CompoundsPhosphoric Triester HydrolasesColloid and Surface ChemistrychemistrySomanHydrolasemedicineDiisopropyl fluorophosphateChemical Warfare AgentsCrystallizationDiisopropyl-fluorophosphatasemedicine.drugNerve agentJournal of the American Chemical Society
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Inside the Hsp90 inhibitors binding mode through induced fit docking

2009

Abstract During the last few decades, the development of new anticancer strategies had to face the instability of many tumors, occurring when the genetic plasticity of cells produces new drug-resistant cancers. It has been shown that a chaperone protein, heat shock protein 90 (Hsp90), is one of the fundamental factors involved in the cell response to stresses, and its role in many biochemical pathways has been demonstrated. Thus, the inhibition of Hsp90 represents a new target of antitumor therapy, since it may influence many specific signaling pathways. The natural antibiotic Geldanamycin is the first Hsp90 inhibitor that has been identified. Nevertheless, more potent and water-soluble sma…

Models MolecularStereochemistryLactams MacrocyclicMolecular Sequence DataComputational biologyCrystallography X-RayLigandsHsp90 inhibitorchemistry.chemical_compoundAdenosine TriphosphateHeat shock proteinCatalytic DomainMaterials ChemistryBenzoquinonesAmino Acid SequenceHSP90 Heat-Shock ProteinsPhysical and Theoretical ChemistrySpectroscopyInduced fitBinding SitesbiologyMolecular StructureHeat shock proteinDrug discoveryActive siteGeldanamycinRadicicolComputer Graphics and Computer-Aided DesignSmall moleculeHsp90Settore CHIM/08 - Chimica FarmaceuticachemistryDocking (molecular)Molecular dockingbiology.proteinGeldanamicynSequence AlignmentProtein Binding
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